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PDBsum entry 2v63

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Oxidoreductase PDB id
2v63
Jmol
Contents
Protein chains
(+ 2 more) 466 a.a.
(+ 2 more) 140 a.a.
Ligands
CAP ×8
EDO ×46
Metals
_MG ×8
Waters ×2892
HEADER    OXIDOREDUCTASE                          13-JUL-07   2V63
TITLE     CRYSTAL STRUCTURE OF RUBISCO FROM CHLAMYDOMONAS REINHARDTII
TITLE    2 WITH A LARGE-SUBUNIT V331A MUTATION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN;
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;
COMPND   4 SYNONYM: RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE LARGE
COMPND   5  CHAIN, RUBISCO LARGE SUBUNIT;
COMPND   6 EC: 4.1.1.39;
COMPND   7 ENGINEERED: YES;
COMPND   8 MUTATION: YES;
COMPND   9 MOL_ID: 2;
COMPND  10 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1;
COMPND  11 CHAIN: I, J, K, L, M, N, O, P;
COMPND  12 SYNONYM: RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE SMALL
COMPND  13  CHAIN, RUBISCO SMALL SUBUNIT 1;
COMPND  14 EC: 4.1.1.39;
COMPND  15 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;
SOURCE   3 ORGANISM_TAXID: 3055;
SOURCE   4 STRAIN: 2137;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PLS-V331A;
SOURCE   8 MOL_ID: 2;
SOURCE   9 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;
SOURCE  10 ORGANISM_TAXID: 3055;
SOURCE  11 STRAIN: 2137;
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  14 EXPRESSION_SYSTEM_PLASMID: PLS-V331A
KEYWDS    LARGE SUBUNIT LOOP 6 MUTATION, CO2/O2 SPECIFICITY, CARBON
KEYWDS   2 DIOXIDE FIXATION, PHOTOSYNTHESIS, TRANSIT PEPTIDE,
KEYWDS   3 PHOTORESPIRATION, METAL-BINDING, HYDROXYLATION,
KEYWDS   4 OXIDOREDUCTASE, METHYLATION, CHLOROPLAST, CALVIN CYCLE,
KEYWDS   5 MONOOXYGENASE, LYASE, RUBISCO, PLASTID, MAGNESIUM,
KEYWDS   6 ACETYLATION
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.KARKEHABADI,S.SATAGOPAN,T.C.TAYLOR,R.J.SPREITZER,
AUTHOR   2 I.ANDERSSON
REVDAT   6   24-FEB-09 2V63    1       VERSN
REVDAT   5   23-OCT-07 2V63    1       REMARK
REVDAT   4   02-OCT-07 2V63    1       JRNL   REMARK
REVDAT   3   28-AUG-07 2V63    1       AUTHOR
REVDAT   2   07-AUG-07 2V63    1       SOURCE REMARK
REVDAT   1   31-JUL-07 2V63    0
JRNL        AUTH   S.KARKEHABADI,S.SATAGOPAN,T.C.TAYLOR,R.J.SPREITZER,
JRNL        AUTH 2 I.ANDERSSON
JRNL        TITL   STRUCTURAL ANALYSIS OF ALTERED LARGE-SUBUNIT LOOP-
JRNL        TITL 2 6-CARBOXY-TERMINUS INTERACTIONS THAT INFLUENCE
JRNL        TITL 3 CATALYTIC EFFICIENCY AND CO2 O2 SPECIFICITY OF
JRNL        TITL 4 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE OXYGENASE
JRNL        REF    BIOCHEMISTRY                  V.  46 11080 2007
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   17824672
JRNL        DOI    10.1021/BI701063F
REMARK   2
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.1
REMARK   3   NUMBER OF REFLECTIONS             : 369935
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.193
REMARK   3   R VALUE            (WORKING SET) : 0.191
REMARK   3   FREE R VALUE                     : 0.214
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 19621
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 17388
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 58.87
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2430
REMARK   3   BIN FREE R VALUE SET COUNT          : 912
REMARK   3   BIN FREE R VALUE                    : 0.2700
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 37813
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 768
REMARK   3   SOLVENT ATOMS            : 2892
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.05
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.44000
REMARK   3    B22 (A**2) : -0.02000
REMARK   3    B33 (A**2) : -0.46000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.05000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.162
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.135
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.088
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.794
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 39483 ; 0.008 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 53456 ; 1.108 ; 1.958
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  4828 ; 5.631 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1859 ;30.604 ;23.168
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  6328 ;13.328 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   319 ;15.644 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  5656 ; 0.080 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 30387 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A): 19533 ; 0.192 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 27022 ; 0.306 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  3203 ; 0.120 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    14 ; 0.024 ; 0.200
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   127 ; 0.291 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    15 ; 0.133 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 24678 ; 0.654 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 38601 ; 1.043 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 16985 ; 1.730 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 14855 ; 2.795 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 16
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A     13       A     438      1
REMARK   3           2     A    440       A     477      1
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   1    A    (A):   3636 ;   .00 ;   .05
REMARK   3   TIGHT THERMAL      1    A (A**2):   3636 ;   .00 ;   .50
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 2
REMARK   3     CHAIN NAMES                    : B A
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     B     13       B     438      1
REMARK   3           1     A     13       A     438      1
REMARK   3           2     B    440       B     477      1
REMARK   3           2     A    440       A     477      1
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   2    B    (A):   3623 ;   .02 ;   .05
REMARK   3   TIGHT THERMAL      2    B (A**2):   3623 ;   .09 ;   .50
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 3
REMARK   3     CHAIN NAMES                    : C A
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     C     13       C     437      1
REMARK   3           1     A     13       A     437      1
REMARK   3           2     C    442       C     477      1
REMARK   3           2     A    442       A     477      1
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   3    C    (A):   3610 ;   .02 ;   .05
REMARK   3   TIGHT THERMAL      3    C (A**2):   3610 ;   .09 ;   .50
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 4
REMARK   3     CHAIN NAMES                    : D A
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     D     13       D     438      1
REMARK   3           1     A     13       A     438      1
REMARK   3           2     D    440       D     477      1
REMARK   3           2     A    440       A     477      1
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   4    D    (A):   3620 ;   .02 ;   .05
REMARK   3   TIGHT THERMAL      4    D (A**2):   3620 ;   .09 ;   .50
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 5
REMARK   3     CHAIN NAMES                    : E A
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     E     13       E     438      1
REMARK   3           1     A     13       A     438      1
REMARK   3           2     E    440       E     477      1
REMARK   3           2     A    440       A     477      1
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   5    E    (A):   3620 ;   .02 ;   .05
REMARK   3   TIGHT THERMAL      5    E (A**2):   3620 ;   .12 ;   .50
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 6
REMARK   3     CHAIN NAMES                    : F A
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     F     13       F     438      1
REMARK   3           1     A     13       A     438      1
REMARK   3           2     F    440       F     477      1
REMARK   3           2     A    440       A     477      1
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   6    F    (A):   3610 ;   .02 ;   .05
REMARK   3   TIGHT THERMAL      6    F (A**2):   3610 ;   .15 ;   .50
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 7
REMARK   3     CHAIN NAMES                    : G A
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     G     13       G     438      1
REMARK   3           1     A     13       A     438      1
REMARK   3           2     G    440       G     477      1
REMARK   3           2     A    440       A     477      1
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   7    G    (A):   3618 ;   .02 ;   .05
REMARK   3   TIGHT THERMAL      7    G (A**2):   3618 ;   .11 ;   .50
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 8
REMARK   3     CHAIN NAMES                    : H A
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     H     13       H     438      1
REMARK   3           1     A     13       A     438      1
REMARK   3           2     H    440       H     477      1
REMARK   3           2     A    440       A     477      1
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   8    H    (A):   3620 ;   .02 ;   .05
REMARK   3   TIGHT THERMAL      8    H (A**2):   3620 ;   .09 ;   .50
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 9
REMARK   3     CHAIN NAMES                    : I
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     I      1       I      83      1
REMARK   3           2     I     85       I     129      1
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   9    I    (A):   1039 ;   .00 ;   .05
REMARK   3   TIGHT THERMAL      9    I (A**2):   1039 ;   .00 ;   .50
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 10
REMARK   3     CHAIN NAMES                    : J I
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     J      1       J      83      1
REMARK   3           1     I      1       I      83      1
REMARK   3           2     J     85       J     129      1
REMARK   3           2     I     85       I     129      1
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL  10    J    (A):   1037 ;   .03 ;   .05
REMARK   3   TIGHT THERMAL     10    J (A**2):   1037 ;   .08 ;   .50
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 11
REMARK   3     CHAIN NAMES                    : K I
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     K      1       K      83      1
REMARK   3           1     I      1       I      83      1
REMARK   3           2     K     85       K     129      1
REMARK   3           2     I     85       I     129      1
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL  11    K    (A):   1037 ;   .02 ;   .05
REMARK   3   TIGHT THERMAL     11    K (A**2):   1037 ;   .09 ;   .50
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 12
REMARK   3     CHAIN NAMES                    : L I
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     L      1       L      83      1
REMARK   3           1     I      1       I      83      1
REMARK   3           2     L     85       L     129      1
REMARK   3           2     I     85       I     129      1
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL  12    L    (A):   1039 ;   .03 ;   .05
REMARK   3   TIGHT THERMAL     12    L (A**2):   1039 ;   .10 ;   .50
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 13
REMARK   3     CHAIN NAMES                    : M I
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     M      1       M      83      1
REMARK   3           1     I      1       I      83      1
REMARK   3           2     M     85       M     129      1
REMARK   3           2     I     85       I     129      1
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL  13    M    (A):   1036 ;   .03 ;   .05
REMARK   3   TIGHT THERMAL     13    M (A**2):   1036 ;   .13 ;   .50
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 14
REMARK   3     CHAIN NAMES                    : N I
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     N      1       N      83      1
REMARK   3           1     I      1       I      83      1
REMARK   3           2     N     85       N     129      1
REMARK   3           2     I     85       I     129      1
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL  14    N    (A):   1038 ;   .02 ;   .05
REMARK   3   TIGHT THERMAL     14    N (A**2):   1038 ;   .12 ;   .50
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 15
REMARK   3     CHAIN NAMES                    : O I
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     O      1       O      83      1
REMARK   3           1     I      1       I      83      1
REMARK   3           2     O     85       O     129      1
REMARK   3           2     I     85       I     129      1
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL  15    O    (A):   1037 ;   .02 ;   .05
REMARK   3   TIGHT THERMAL     15    O (A**2):   1037 ;   .08 ;   .50
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 16
REMARK   3     CHAIN NAMES                    : P I
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     P      1       P      83      1
REMARK   3           1     I      1       I      83      1
REMARK   3           2     P     85       P     129      1
REMARK   3           2     I     85       I     129      1
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL  16    P    (A):   1039 ;   .02 ;   .05
REMARK   3   TIGHT THERMAL     16    P (A**2):   1039 ;   .12 ;   .50
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 2V63 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-JUL-07.
REMARK 100 THE PDBE ID CODE IS EBI-33172.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-MAY-03
REMARK 200  TEMPERATURE           (KELVIN) : 200
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9392
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 389935
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.80
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.00
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.4
REMARK 200  DATA REDUNDANCY                : 14.8
REMARK 200  R MERGE                    (I) : 0.23
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 16.50
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.83
REMARK 200  COMPLETENESS FOR SHELL     (%) : 60.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.46
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.40
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1GK8
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 38.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA):2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       88.72300
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE:  1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXADECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 127910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 153680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -728.8 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,
REMARK 350                    AND CHAINS: J, K, L, M, N, O, P
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, VAL 331 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, VAL 331 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, VAL 331 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, VAL 331 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN E, VAL 331 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN F, VAL 331 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN G, VAL 331 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN H, VAL 331 TO ALA
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A     1
REMARK 465     VAL A     2
REMARK 465     PRO A     3
REMARK 465     GLN A     4
REMARK 465     THR A     5
REMARK 465     GLU A     6
REMARK 465     THR A     7
REMARK 465     LYS A     8
REMARK 465     LEU A   475
REMARK 465     MET B     1
REMARK 465     VAL B     2
REMARK 465     PRO B     3
REMARK 465     GLN B     4
REMARK 465     THR B     5
REMARK 465     GLU B     6
REMARK 465     THR B     7
REMARK 465     LYS B     8
REMARK 465     LEU B   475
REMARK 465     MET C     1
REMARK 465     VAL C     2
REMARK 465     PRO C     3
REMARK 465     GLN C     4
REMARK 465     THR C     5
REMARK 465     GLU C     6
REMARK 465     THR C     7
REMARK 465     LYS C     8
REMARK 465     LEU C   475
REMARK 465     MET D     1
REMARK 465     VAL D     2
REMARK 465     PRO D     3
REMARK 465     GLN D     4
REMARK 465     THR D     5
REMARK 465     GLU D     6
REMARK 465     THR D     7
REMARK 465     LYS D     8
REMARK 465     ALA D     9
REMARK 465     GLY D    10
REMARK 465     LEU D   475
REMARK 465     MET E     1
REMARK 465     VAL E     2
REMARK 465     PRO E     3
REMARK 465     GLN E     4
REMARK 465     THR E     5
REMARK 465     GLU E     6
REMARK 465     THR E     7
REMARK 465     LYS E     8
REMARK 465     ALA E     9
REMARK 465     GLY E    10
REMARK 465     LEU E   475
REMARK 465     MET F     1
REMARK 465     VAL F     2
REMARK 465     PRO F     3
REMARK 465     GLN F     4
REMARK 465     THR F     5
REMARK 465     GLU F     6
REMARK 465     THR F     7
REMARK 465     LYS F     8
REMARK 465     LEU F   475
REMARK 465     MET G     1
REMARK 465     VAL G     2
REMARK 465     PRO G     3
REMARK 465     GLN G     4
REMARK 465     THR G     5
REMARK 465     GLU G     6
REMARK 465     THR G     7
REMARK 465     LYS G     8
REMARK 465     LEU G   475
REMARK 465     MET H     1
REMARK 465     VAL H     2
REMARK 465     PRO H     3
REMARK 465     GLN H     4
REMARK 465     THR H     5
REMARK 465     GLU H     6
REMARK 465     THR H     7
REMARK 465     LYS H     8
REMARK 465     LEU H   475
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    GLU G    93  -  O    HOH G  2058              2.15
REMARK 500   O    PRO I    20  -  O    HOH I  2010              2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    SER A  62      -80.48   -138.75
REMARK 500    ASN A 207      -91.39   -119.63
REMARK 500    MET A 212      107.84   -165.91
REMARK 500    MET A 297       -8.68     86.32
REMARK 500    ALA A 331      -44.89     73.92
REMARK 500    SER B  62      -80.29   -137.18
REMARK 500    ASN B 207      -89.56   -121.03
REMARK 500    MET B 212      107.30   -165.96
REMARK 500    MET B 297       -8.13     86.46
REMARK 500    ALA B 331      -45.72     75.38
REMARK 500    ASP B 357       89.92   -158.31
REMARK 500    SER C  62      -81.52   -138.78
REMARK 500    ASN C 207      -89.20   -119.69
REMARK 500    MET C 212      106.63   -166.10
REMARK 500    ALA C 296      130.98    -39.50
REMARK 500    MET C 297       -8.47     87.63
REMARK 500    ALA C 331      -46.61     72.82
REMARK 500    ASP C 357       89.87   -158.38
REMARK 500    SER D  62      -81.70   -137.81
REMARK 500    ASN D 207      -90.69   -119.57
REMARK 500    MET D 212      109.94   -164.83
REMARK 500    ALA D 296      131.84    -38.70
REMARK 500    MET D 297      -11.06     86.71
REMARK 500    ALA D 331      -44.59     76.12
REMARK 500    SER E  62      -81.43   -141.96
REMARK 500    ASN E 207      -92.18   -119.57
REMARK 500    MET E 212      109.88   -162.16
REMARK 500    ALA E 296      130.78    -39.93
REMARK 500    MET E 297       -9.13     87.21
REMARK 500    ALA E 331      -42.96     73.74
REMARK 500    SER F  62      -78.46   -138.37
REMARK 500    ASN F 207      -90.38   -123.61
REMARK 500    MET F 212      105.83   -164.64
REMARK 500    MET F 297       -7.31     84.61
REMARK 500    ALA F 331      -45.54     72.13
REMARK 500    ASP F 357       90.65   -160.32
REMARK 500    SER G  62      -80.59   -139.74
REMARK 500    ASN G 207      -92.41   -121.87
REMARK 500    MET G 212      107.41   -167.13
REMARK 500    ALA G 296      132.46    -36.85
REMARK 500    MET G 297       -8.51     86.96
REMARK 500    ALA G 331      -45.15     72.66
REMARK 500    SER H  62      -81.90   -135.62
REMARK 500    ASN H 207      -92.48   -117.23
REMARK 500    MET H 212      108.26   -164.19
REMARK 500    MET H 297       -6.63     87.03
REMARK 500    ALA H 331      -43.84     75.42
REMARK 500    ASP H 357       89.64   -160.46
REMARK 500    GLU I  13     -142.01     57.95
REMARK 500    PHE I  15       -1.08     82.86
REMARK 500    LYS I  77     -123.79     56.53
REMARK 500    GLU J  13     -140.57     55.34
REMARK 500    PHE J  15       -0.78     81.67
REMARK 500    LYS J  77     -123.45     54.96
REMARK 500    GLU K  13     -140.82     58.57
REMARK 500    PHE K  15       -1.78     82.37
REMARK 500    LYS K  77     -121.87     53.05
REMARK 500    GLU L  13     -140.43     56.41
REMARK 500    PHE L  15       -0.05     84.31
REMARK 500    LYS L  77     -123.54     56.81
REMARK 500    GLU M  13     -141.86     59.27
REMARK 500    PHE M  15       -0.99     82.43
REMARK 500    LYS M  77     -124.49     56.74
REMARK 500    PHE N  12       44.63   -141.13
REMARK 500    GLU N  13     -141.27     59.79
REMARK 500    PHE N  15       -0.66     82.95
REMARK 500    LYS N  77     -124.32     56.38
REMARK 500    PHE O  12       48.83   -140.19
REMARK 500    GLU O  13     -142.02     56.14
REMARK 500    PHE O  15        1.62     82.39
REMARK 500    LYS O  77     -123.34     55.54
REMARK 500    PHE P  12       47.95   -143.04
REMARK 500    GLU P  13     -142.69     57.40
REMARK 500    PHE P  15       -0.31     81.86
REMARK 500    LYS P  77     -124.07     58.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE)
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 477  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX A 201   OQ1
REMARK 620 2 ASP A 203   OD1  90.2
REMARK 620 3 CAP A 476   O2   94.4 104.3
REMARK 620 4 GLU A 204   OE1  88.5  92.2 163.2
REMARK 620 5 CAP A 476   O3   86.4 176.5  75.1  88.6
REMARK 620 6 CAP A 476   O7  169.3  96.9  76.1  99.1  86.3
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG B 476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX B 201   OQ1
REMARK 620 2 CAP B 477   O2   98.3
REMARK 620 3 CAP B 477   O3   91.0  75.9
REMARK 620 4 ASP B 203   OD1  90.4 101.4 177.1
REMARK 620 5 GLU B 204   OE1  90.7 163.2  89.8  92.7
REMARK 620 6 CAP B 477   O7  171.1  73.3  84.2  94.1  96.8
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG C 476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP C 477   O3
REMARK 620 2 KCX C 201   OQ1  89.7
REMARK 620 3 ASP C 203   OD1 177.7  90.9
REMARK 620 4 CAP C 477   O2   74.9  94.7 102.8
REMARK 620 5 GLU C 204   OE1  89.3  91.5  92.9 163.0
REMARK 620 6 CAP C 477   O7   82.3 166.5  96.7  72.9  99.1
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG D 476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 203   OD1
REMARK 620 2 GLU D 204   OE1  94.1
REMARK 620 3 CAP D 477   O2  103.3 161.1
REMARK 620 4 CAP D 477   O7   95.1  97.4  74.0
REMARK 620 5 KCX D 201   OQ1  91.5  91.1  95.8 168.8
REMARK 620 6 CAP D 477   O3  177.7  88.0  74.7  85.3  87.7
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG E 476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP E 477   O2
REMARK 620 2 CAP E 477   O3   74.0
REMARK 620 3 CAP E 477   O7   76.4  88.0
REMARK 620 4 ASP E 203   OD1 103.6 175.5  95.2
REMARK 620 5 GLU E 204   OE1 162.8  89.8  97.6  92.9
REMARK 620 6 KCX E 201   OQ1  93.4  84.6 168.8  91.8  90.7
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG F 476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 203   OD1
REMARK 620 2 CAP F 477   O2  105.4
REMARK 620 3 CAP F 477   O7   94.9  72.8
REMARK 620 4 KCX F 201   OQ1  91.9  95.8 168.0
REMARK 620 5 GLU F 204   OE1  91.0 162.6 100.6  89.2
REMARK 620 6 CAP F 477   O3  179.5  75.0  85.5  87.8  88.6
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG G 476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 203   OD1
REMARK 620 2 CAP G 477   O2  101.2
REMARK 620 3 CAP G 477   O7   95.6  73.2
REMARK 620 4 KCX G 201   OQ1  91.0  93.6 166.1
REMARK 620 5 GLU G 204   OE1  95.6 162.3  99.9  91.6
REMARK 620 6 CAP G 477   O3  174.8  73.6  83.7  88.5  89.6
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG H 476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP H 477   O3
REMARK 620 2 KCX H 201   OQ1  87.5
REMARK 620 3 CAP H 477   O2   74.6  95.0
REMARK 620 4 CAP H 477   O7   87.4 170.8  76.3
REMARK 620 5 ASP H 203   OD1 176.2  89.4 103.5  95.4
REMARK 620 6 GLU H 204   OE1  89.4  90.0 162.9  97.5  92.8
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG C 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP C 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG D 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP D 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG E 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG F 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP F 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG G 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP G 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG H 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP H 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1142
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1475
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1475
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO J1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1475
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1475
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO J1142
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO P1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO N1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO N1142
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO L1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO L1142
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO I1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1142
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO M1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO M1142
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1475
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1475
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1475
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1476
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1UW9   RELATED DB: PDB
REMARK 900  L290F-A222T CHLAMYDOMONAS RUBISCO MUTANT
REMARK 900 RELATED ID: 1IR2   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF ACTIVATED RIBULOSE-1,5
REMARK 900  -BISPHOSPHATECARBOXYLASE/OXYGENASE (RUBISCO) FROM
REMARK 900   GREEN ALGA,CHLAMYDOMONAS REINHARDTII COMPLEXED
REMARK 900   WITH 2-CARBOXYARABINITOL-1,5-BISPHOSPHATE (
REMARK 900  2-CABP)
REMARK 900 RELATED ID: 1UZD   RELATED DB: PDB
REMARK 900  CHLAMYDOMONAS,SPINACH CHIMERIC RUBISCO
REMARK 900 RELATED ID: 1UZH   RELATED DB: PDB
REMARK 900  A CHIMERIC CHLAMYDOMONAS, SPINACH RUBISCO
REMARK 900  ENZYME
REMARK 900 RELATED ID: 1GK8   RELATED DB: PDB
REMARK 900  RUBISCO FROM CHLAMYDOMONAS REINHARDTII
REMARK 900 RELATED ID: 2V67   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII
REMARK 900  RUBISCO WITH A LARGE-SUBUNIT SUPRESSOR
REMARK 900  MUTATION T342I
REMARK 900 RELATED ID: 2V68   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII
REMARK 900  RUBISCO WITH LARGE-SUBUNIT MUTATIONS V331A,
REMARK 900  T342I
REMARK 900 RELATED ID: 2V69   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII
REMARK 900  RUBISCO WITH A LARGE-SUBUNIT MUTATION D473E
REMARK 900 RELATED ID: 2V6A   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII
REMARK 900  RUBISCO WITH LARGE-SUBUNIT MUTATIONS V331A,
REMARK 900  G344S
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE UNIPROT DATABASE ENTRY FOR THIS SEQUENCE (P00877)
REMARK 999 HAS A VARIANT (LEU46PRO) WHICH OCCURS IN STRAIN 21GR
REMARK 999 AND 2137.
DBREF  2V63 A    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  2V63 B    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  2V63 C    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  2V63 D    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  2V63 E    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  2V63 F    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  2V63 G    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  2V63 H    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  2V63 I    1   140  UNP    P00873   RBS1_CHLRE      46    185
DBREF  2V63 J    1   140  UNP    P00873   RBS1_CHLRE      46    185
DBREF  2V63 K    1   140  UNP    P00873   RBS1_CHLRE      46    185
DBREF  2V63 L    1   140  UNP    P00873   RBS1_CHLRE      46    185
DBREF  2V63 M    1   140  UNP    P00873   RBS1_CHLRE      46    185
DBREF  2V63 N    1   140  UNP    P00873   RBS1_CHLRE      46    185
DBREF  2V63 O    1   140  UNP    P00873   RBS1_CHLRE      46    185
DBREF  2V63 P    1   140  UNP    P00873   RBS1_CHLRE      46    185
SEQADV 2V63 PRO A   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 2V63 ALA A  331  UNP  P00877    VAL   331 ENGINEERED MUTATION
SEQADV 2V63 PRO B   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 2V63 ALA B  331  UNP  P00877    VAL   331 ENGINEERED MUTATION
SEQADV 2V63 PRO C   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 2V63 ALA C  331  UNP  P00877    VAL   331 ENGINEERED MUTATION
SEQADV 2V63 PRO D   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 2V63 ALA D  331  UNP  P00877    VAL   331 ENGINEERED MUTATION
SEQADV 2V63 PRO E   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 2V63 ALA E  331  UNP  P00877    VAL   331 ENGINEERED MUTATION
SEQADV 2V63 PRO F   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 2V63 ALA F  331  UNP  P00877    VAL   331 ENGINEERED MUTATION
SEQADV 2V63 PRO G   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 2V63 ALA G  331  UNP  P00877    VAL   331 ENGINEERED MUTATION
SEQADV 2V63 PRO H   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 2V63 ALA H  331  UNP  P00877    VAL   331 ENGINEERED MUTATION
SEQRES   1 A  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 A  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 A  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 A  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 A  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 A  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 A  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 A  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 A  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 A  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 A  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 A  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 A  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 A  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 A  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 A  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 A  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 A  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 A  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 A  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 A  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 A  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 A  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 A  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 A  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 A  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 A  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES  28 A  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 A  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 A  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 A  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 A  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 A  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 A  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 A  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 A  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 A  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 B  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 B  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 B  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 B  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 B  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 B  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 B  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 B  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 B  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 B  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 B  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 B  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 B  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 B  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 B  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 B  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 B  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 B  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 B  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 B  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 B  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 B  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 B  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 B  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 B  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 B  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 B  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES  28 B  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 B  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 B  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 B  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 B  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 B  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 B  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 B  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 B  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 B  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 C  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 C  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 C  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 C  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 C  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 C  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 C  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 C  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 C  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 C  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 C  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 C  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 C  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 C  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 C  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 C  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 C  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 C  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 C  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 C  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 C  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 C  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 C  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 C  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 C  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 C  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 C  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES  28 C  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 C  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 C  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 C  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 C  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 C  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 C  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 C  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 C  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 C  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 D  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 D  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 D  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 D  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 D  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 D  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 D  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 D  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 D  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 D  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 D  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 D  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 D  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 D  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 D  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 D  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 D  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 D  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 D  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 D  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 D  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 D  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 D  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 D  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 D  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 D  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 D  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES  28 D  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 D  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 D  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 D  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 D  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 D  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 D  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 D  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 D  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 D  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 E  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 E  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 E  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 E  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 E  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 E  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 E  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 E  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 E  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 E  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 E  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 E  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 E  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 E  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 E  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 E  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 E  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 E  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 E  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 E  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 E  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 E  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 E  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 E  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 E  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 E  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 E  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES  28 E  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 E  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 E  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 E  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 E  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 E  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 E  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 E  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 E  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 E  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 F  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 F  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 F  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 F  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 F  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 F  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 F  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 F  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 F  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 F  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 F  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 F  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 F  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 F  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 F  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 F  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 F  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 F  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 F  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 F  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 F  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 F  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 F  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 F  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 F  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 F  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 F  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES  28 F  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 F  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 F  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 F  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 F  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 F  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 F  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 F  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 F  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 F  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 G  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 G  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 G  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 G  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 G  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 G  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 G  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 G  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 G  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 G  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 G  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 G  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 G  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 G  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 G  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 G  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 G  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 G  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 G  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 G  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 G  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 G  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 G  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 G  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 G  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 G  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 G  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES  28 G  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 G  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 G  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 G  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 G  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 G  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 G  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 G  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 G  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 G  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 H  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 H  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 H  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 H  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 H  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 H  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 H  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 H  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 H  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 H  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 H  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 H  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 H  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 H  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 H  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 H  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 H  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 H  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 H  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 H  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 H  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 H  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 H  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 H  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 H  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 H  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 H  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES  28 H  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 H  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 H  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 H  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 H  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 H  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 H  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 H  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 H  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 H  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 I  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 I  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 I  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 I  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES   5 I  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES   6 I  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES   7 I  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES   8 I  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES   9 I  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES  10 I  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG
SEQRES  11 I  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL
SEQRES   1 J  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 J  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 J  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 J  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES   5 J  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES   6 J  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES   7 J  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES   8 J  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES   9 J  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES  10 J  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG
SEQRES  11 J  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL
SEQRES   1 K  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 K  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 K  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 K  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES   5 K  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES   6 K  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES   7 K  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES   8 K  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES   9 K  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES  10 K  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG
SEQRES  11 K  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL
SEQRES   1 L  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 L  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 L  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 L  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES   5 L  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES   6 L  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES   7 L  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES   8 L  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES   9 L  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES  10 L  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG
SEQRES  11 L  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL
SEQRES   1 M  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 M  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 M  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 M  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES   5 M  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES   6 M  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES   7 M  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES   8 M  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES   9 M  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES  10 M  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG
SEQRES  11 M  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL
SEQRES   1 N  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 N  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 N  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 N  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES   5 N  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES   6 N  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES   7 N  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES   8 N  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES   9 N  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES  10 N  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG
SEQRES  11 N  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL
SEQRES   1 O  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 O  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 O  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 O  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES   5 O  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES   6 O  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES   7 O  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES   8 O  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES   9 O  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES  10 O  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG
SEQRES  11 O  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL
SEQRES   1 P  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 P  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 P  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 P  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES   5 P  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES   6 P  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES   7 P  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES   8 P  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES   9 P  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES  10 P  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG
SEQRES  11 P  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL
MODRES 2V63 HYP A  104  PRO  4-HYDROXYPROLINE
MODRES 2V63 HYP A  151  PRO  4-HYDROXYPROLINE
MODRES 2V63 KCX A  201  LYS  LYSYL-CARBAMATE
MODRES 2V63 SMC A  256  CYS  S-METHYLCYSTEINE
MODRES 2V63 SMC A  369  CYS  S-METHYLCYSTEINE
MODRES 2V63 HYP B  104  PRO  4-HYDROXYPROLINE
MODRES 2V63 HYP B  151  PRO  4-HYDROXYPROLINE
MODRES 2V63 KCX B  201  LYS  LYSYL-CARBAMATE
MODRES 2V63 SMC B  256  CYS  S-METHYLCYSTEINE
MODRES 2V63 SMC B  369  CYS  S-METHYLCYSTEINE
MODRES 2V63 HYP C  104  PRO  4-HYDROXYPROLINE
MODRES 2V63 HYP C  151  PRO  4-HYDROXYPROLINE
MODRES 2V63 KCX C  201  LYS  LYSYL-CARBAMATE
MODRES 2V63 SMC C  256  CYS  S-METHYLCYSTEINE
MODRES 2V63 SMC C  369  CYS  S-METHYLCYSTEINE
MODRES 2V63 HYP D  104  PRO  4-HYDROXYPROLINE
MODRES 2V63 HYP D  151  PRO  4-HYDROXYPROLINE
MODRES 2V63 KCX D  201  LYS  LYSYL-CARBAMATE
MODRES 2V63 SMC D  256  CYS  S-METHYLCYSTEINE
MODRES 2V63 SMC D  369  CYS  S-METHYLCYSTEINE
MODRES 2V63 HYP E  104  PRO  4-HYDROXYPROLINE
MODRES 2V63 HYP E  151  PRO  4-HYDROXYPROLINE
MODRES 2V63 KCX E  201  LYS  LYSYL-CARBAMATE
MODRES 2V63 SMC E  256  CYS  S-METHYLCYSTEINE
MODRES 2V63 SMC E  369  CYS  S-METHYLCYSTEINE
MODRES 2V63 HYP F  104  PRO  4-HYDROXYPROLINE
MODRES 2V63 HYP F  151  PRO  4-HYDROXYPROLINE
MODRES 2V63 KCX F  201  LYS  LYSYL-CARBAMATE
MODRES 2V63 SMC F  256  CYS  S-METHYLCYSTEINE
MODRES 2V63 SMC F  369  CYS  S-METHYLCYSTEINE
MODRES 2V63 HYP G  104  PRO  4-HYDROXYPROLINE
MODRES 2V63 HYP G  151  PRO  4-HYDROXYPROLINE
MODRES 2V63 KCX G  201  LYS  LYSYL-CARBAMATE
MODRES 2V63 SMC G  256  CYS  S-METHYLCYSTEINE
MODRES 2V63 SMC G  369  CYS  S-METHYLCYSTEINE
MODRES 2V63 HYP H  104  PRO  4-HYDROXYPROLINE
MODRES 2V63 HYP H  151  PRO  4-HYDROXYPROLINE
MODRES 2V63 KCX H  201  LYS  LYSYL-CARBAMATE
MODRES 2V63 SMC H  256  CYS  S-METHYLCYSTEINE
MODRES 2V63 SMC H  369  CYS  S-METHYLCYSTEINE
MODRES 2V63 MME I    1  MET  N-METHYL METHIONINE
MODRES 2V63 MME J    1  MET  N-METHYL METHIONINE
MODRES 2V63 MME K    1  MET  N-METHYL METHIONINE
MODRES 2V63 MME L    1  MET  N-METHYL METHIONINE
MODRES 2V63 MME M    1  MET  N-METHYL METHIONINE
MODRES 2V63 MME N    1  MET  N-METHYL METHIONINE
MODRES 2V63 MME O    1  MET  N-METHYL METHIONINE
MODRES 2V63 MME P    1  MET  N-METHYL METHIONINE
HET    HYP  A 104       8
HET    HYP  A 151       8
HET    KCX  A 201      12
HET    SMC  A 256       7
HET    SMC  A 369       7
HET    CAP  A 476      21
HET     MG  A 477       1
HET     MG  B 476       1
HET    CAP  B 477      21
HET     MG  C 476       1
HET    CAP  C 477      21
HET     MG  D 476       1
HET    CAP  D 477      21
HET     MG  E 476       1
HET    CAP  E 477      21
HET     MG  F 476       1
HET    CAP  F 477      21
HET     MG  G 476       1
HET    CAP  G 477      21
HET     MG  H 476       1
HET    CAP  H 477      21
HET    HYP  B 104       8
HET    HYP  B 151       8
HET    KCX  B 201      12
HET    SMC  B 256       7
HET    SMC  B 369       7
HET    HYP  C 104       8
HET    HYP  C 151       8
HET    KCX  C 201      12
HET    SMC  C 256       7
HET    SMC  C 369       7
HET    HYP  D 104       8
HET    HYP  D 151       8
HET    KCX  D 201      12
HET    SMC  D 256       7
HET    SMC  D 369       7
HET    HYP  E 104       8
HET    HYP  E 151       8
HET    KCX  E 201      12
HET    SMC  E 256       7
HET    SMC  E 369       7
HET    HYP  F 104       8
HET    HYP  F 151       8
HET    KCX  F 201      12
HET    SMC  F 256       7
HET    SMC  F 369       7
HET    HYP  G 104       8
HET    HYP  G 151       8
HET    KCX  G 201      12
HET    SMC  G 256       7
HET    SMC  G 369       7
HET    HYP  H 104       8
HET    HYP  H 151       8
HET    KCX  H 201      12
HET    SMC  H 256       7
HET    SMC  H 369       7
HET    MME  I   1       9
HET    MME  J   1       9
HET    MME  K   1       9
HET    MME  L   1       9
HET    MME  M   1       9
HET    MME  N   1       9
HET    MME  O   1       9
HET    MME  P   1       9
HET    EDO  A1477       4
HET    EDO  A1478       4
HET    EDO  A1479       4
HET    EDO  H1477       4
HET    EDO  H1478       4
HET    EDO  O1141       4
HET    EDO  O1142       4
HET    EDO  C1475       4
HET    EDO  K1141       4
HET    EDO  B1475       4
HET    EDO  B1476       4
HET    EDO  B1477       4
HET    EDO  B1478       4
HET    EDO  J1141       4
HET    EDO  G1479       4
HET    EDO  D1475       4
HET    EDO  D1476       4
HET    EDO  E1475       4
HET    EDO  E1477       4
HET    EDO  J1142       4
HET    EDO  D1477       4
HET    EDO  D1478       4
HET    EDO  P1141       4
HET    EDO  N1141       4
HET    EDO  N1142       4
HET    EDO  L1141       4
HET    EDO  L1142       4
HET    EDO  A1480       4
HET    EDO  C1477       4
HET    EDO  C1478       4
HET    EDO  C1479       4
HET    EDO  G1480       4
HET    EDO  I1141       4
HET    EDO  K1142       4
HET    EDO  M1141       4
HET    EDO  M1142       4
HET    EDO  C1476       4
HET    EDO  H1475       4
HET    EDO  H1476       4
HET    EDO  G1475       4
HET    EDO  G1476       4
HET    EDO  G1477       4
HET    EDO  G1478       4
HET    EDO  E1476       4
HET    EDO  F1475       4
HET    EDO  F1476       4
HETNAM     CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE
HETNAM     HYP 4-HYDROXYPROLINE
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID
HETNAM     SMC S-METHYLCYSTEINE
HETNAM     MME N-METHYL METHIONINE
HETNAM     EDO 1,2-ETHANEDIOL
HETNAM      MG MAGNESIUM ION
HETSYN     EDO ETHYLENE GLYCOL
FORMUL  17  HYP    16(C5 H9 N O3)
FORMUL  18  KCX    8(C7 H14 N2 O4)
FORMUL  19  SMC    16(C4 H9 N O2 S)
FORMUL  20  MME    8(C6 H13 N O2 S)
FORMUL  21  EDO    46(C2 H6 O2)
FORMUL  22   MG    8(MG 2+)
FORMUL  23  CAP    8(C6 H14 O13 P2)
FORMUL  24  HOH   *2892(H2 O1)
HELIX    1   1 TYR A   20  TYR A   25  1                                   6
HELIX    2   2 PRO A   49  SER A   61  1                                  13
HELIX    3   3 VAL A   69  THR A   75  5                                   7
HELIX    4   4 SER A   76  LYS A   81  1                                   6
HELIX    5   5 HYP A  104  PHE A  108  5                                   5
HELIX    6   6 SER A  112  GLY A  122  1                                  11
HELIX    7   7 ASN A  123  GLY A  126  5                                   4
HELIX    8   8 PRO A  141  LYS A  146  1                                   6
HELIX    9   9 GLY A  154  ASN A  163  1                                  10
HELIX   10  10 SER A  181  GLY A  195  1                                  15
HELIX   11  11 ARG A  213  GLY A  233  1                                  21
HELIX   12  12 THR A  246  VAL A  255  1                                  10
HELIX   13  13 TYR A  269  GLY A  288  1                                  20
HELIX   14  14 MET A  297  ARG A  303  1                                   7
HELIX   15  15 HIS A  310  GLY A  322  1                                  13
HELIX   16  16 GLU A  338  ASP A  351  1                                  14
HELIX   17  17 ARG A  358  GLY A  361  5                                   4
HELIX   18  18 HIS A  383  TRP A  385  5                                   3
HELIX   19  19 HIS A  386  GLY A  395  1                                  10
HELIX   20  20 GLY A  403  GLY A  408  1                                   6
HELIX   21  21 GLY A  412  GLU A  433  1                                  22
HELIX   22  22 ASP A  436  LYS A  463  1                                  28
HELIX   23  23 TYR B   20  TYR B   25  1                                   6
HELIX   24  24 PRO B   49  SER B   61  1                                  13
HELIX   25  25 VAL B   69  THR B   75  5                                   7
HELIX   26  26 SER B   76  LYS B   81  1                                   6
HELIX   27  27 HYP B  104  PHE B  108  5                                   5
HELIX   28  28 SER B  112  GLY B  122  1                                  11
HELIX   29  29 ASN B  123  GLY B  126  5                                   4
HELIX   30  30 PRO B  141  LYS B  146  1                                   6
HELIX   31  31 GLY B  154  ASN B  163  1                                  10
HELIX   32  32 SER B  181  GLY B  195  1                                  15
HELIX   33  33 ARG B  213  GLY B  233  1                                  21
HELIX   34  34 THR B  246  VAL B  255  1                                  10
HELIX   35  35 TYR B  269  GLY B  288  1                                  20
HELIX   36  36 MET B  297  ARG B  303  1                                   7
HELIX   37  37 HIS B  310  GLY B  322  1                                  13
HELIX   38  38 GLU B  338  ASP B  351  1                                  14
HELIX   39  39 ARG B  358  GLY B  361  5                                   4
HELIX   40  40 HIS B  383  TRP B  385  5                                   3
HELIX   41  41 HIS B  386  GLY B  395  1                                  10
HELIX   42  42 GLY B  403  GLY B  408  1                                   6
HELIX   43  43 GLY B  412  GLU B  433  1                                  22
HELIX   44  44 ASP B  436  LYS B  463  1                                  28
HELIX   45  45 TYR C   20  TYR C   25  1                                   6
HELIX   46  46 PRO C   49  SER C   61  1                                  13
HELIX   47  47 VAL C   69  THR C   75  5                                   7
HELIX   48  48 SER C   76  LYS C   81  1                                   6
HELIX   49  49 HYP C  104  PHE C  108  5                                   5
HELIX   50  50 SER C  112  GLY C  122  1                                  11
HELIX   51  51 ASN C  123  GLY C  126  5                                   4
HELIX   52  52 PRO C  141  LYS C  146  1                                   6
HELIX   53  53 GLY C  154  ASN C  163  1                                  10
HELIX   54  54 SER C  181  GLY C  195  1                                  15
HELIX   55  55 ARG C  213  GLY C  233  1                                  21
HELIX   56  56 THR C  246  VAL C  255  1                                  10
HELIX   57  57 TYR C  269  GLY C  288  1                                  20
HELIX   58  58 MET C  297  ARG C  303  1                                   7
HELIX   59  59 HIS C  310  GLY C  322  1                                  13
HELIX   60  60 GLU C  338  ASP C  351  1                                  14
HELIX   61  61 ARG C  358  GLY C  361  5                                   4
HELIX   62  62 HIS C  383  TRP C  385  5                                   3
HELIX   63  63 HIS C  386  GLY C  395  1                                  10
HELIX   64  64 GLY C  403  GLY C  408  1                                   6
HELIX   65  65 GLY C  412  GLU C  433  1                                  22
HELIX   66  66 GLU C  440  SER C  452  1                                  13
HELIX   67  67 SER C  452  LYS C  463  1                                  12
HELIX   68  68 TYR D   20  TYR D   25  1                                   6
HELIX   69  69 PRO D   49  SER D   61  1                                  13
HELIX   70  70 VAL D   69  THR D   75  5                                   7
HELIX   71  71 SER D   76  LYS D   81  1                                   6
HELIX   72  72 HYP D  104  PHE D  108  5                                   5
HELIX   73  73 SER D  112  GLY D  122  1                                  11
HELIX   74  74 ASN D  123  GLY D  126  5                                   4
HELIX   75  75 PRO D  141  LYS D  146  1                                   6
HELIX   76  76 GLY D  154  ASN D  163  1                                  10
HELIX   77  77 SER D  181  GLY D  195  1                                  15
HELIX   78  78 ARG D  213  GLY D  233  1                                  21
HELIX   79  79 THR D  246  VAL D  255  1                                  10
HELIX   80  80 TYR D  269  GLY D  288  1                                  20
HELIX   81  81 MET D  297  ARG D  303  1                                   7
HELIX   82  82 HIS D  310  GLY D  322  1                                  13
HELIX   83  83 GLU D  338  ASP D  351  1                                  14
HELIX   84  84 ARG D  358  GLY D  361  5                                   4
HELIX   85  85 HIS D  383  TRP D  385  5                                   3
HELIX   86  86 HIS D  386  GLY D  395  1                                  10
HELIX   87  87 GLY D  403  GLY D  408  1                                   6
HELIX   88  88 GLY D  412  GLU D  433  1                                  22
HELIX   89  89 ASP D  436  LYS D  463  1                                  28
HELIX   90  90 TYR E   20  TYR E   25  1                                   6
HELIX   91  91 PRO E   49  SER E   61  1                                  13
HELIX   92  92 VAL E   69  THR E   75  5                                   7
HELIX   93  93 SER E   76  LYS E   81  1                                   6
HELIX   94  94 HYP E  104  PHE E  108  5                                   5
HELIX   95  95 SER E  112  GLY E  122  1                                  11
HELIX   96  96 ASN E  123  GLY E  126  5                                   4
HELIX   97  97 PRO E  141  LYS E  146  1                                   6
HELIX   98  98 GLY E  154  ASN E  163  1                                  10
HELIX   99  99 SER E  181  GLY E  195  1                                  15
HELIX  100 100 ARG E  213  GLY E  233  1                                  21
HELIX  101 101 THR E  246  VAL E  255  1                                  10
HELIX  102 102 TYR E  269  GLY E  288  1                                  20
HELIX  103 103 MET E  297  ARG E  303  1                                   7
HELIX  104 104 HIS E  310  GLY E  322  1                                  13
HELIX  105 105 GLU E  338  ASP E  351  1                                  14
HELIX  106 106 ARG E  358  GLY E  361  5                                   4
HELIX  107 107 HIS E  383  TRP E  385  5                                   3
HELIX  108 108 HIS E  386  GLY E  395  1                                  10
HELIX  109 109 GLY E  403  GLY E  408  1                                   6
HELIX  110 110 GLY E  412  GLU E  433  1                                  22
HELIX  111 111 ASP E  436  LYS E  463  1                                  28
HELIX  112 112 TYR F   20  TYR F   25  1                                   6
HELIX  113 113 PRO F   49  SER F   61  1                                  13
HELIX  114 114 VAL F   69  THR F   75  5                                   7
HELIX  115 115 SER F   76  LYS F   81  1                                   6
HELIX  116 116 HYP F  104  PHE F  108  5                                   5
HELIX  117 117 SER F  112  GLY F  122  1                                  11
HELIX  118 118 ASN F  123  GLY F  126  5                                   4
HELIX  119 119 PRO F  141  LYS F  146  1                                   6
HELIX  120 120 GLY F  154  ASN F  163  1                                  10
HELIX  121 121 SER F  181  GLY F  195  1                                  15
HELIX  122 122 ARG F  213  GLY F  233  1                                  21
HELIX  123 123 THR F  246  VAL F  255  1                                  10
HELIX  124 124 TYR F  269  GLY F  288  1                                  20
HELIX  125 125 MET F  297  ARG F  303  1                                   7
HELIX  126 126 HIS F  310  GLY F  322  1                                  13
HELIX  127 127 GLU F  338  ASP F  351  1                                  14
HELIX  128 128 ARG F  358  GLY F  361  5                                   4
HELIX  129 129 HIS F  383  TRP F  385  5                                   3
HELIX  130 130 HIS F  386  GLY F  395  1                                  10
HELIX  131 131 GLY F  403  GLY F  408  1                                   6
HELIX  132 132 GLY F  412  GLU F  433  1                                  22
HELIX  133 133 ASP F  436  LYS F  463  1                                  28
HELIX  134 134 TYR G   20  TYR G   25  1                                   6
HELIX  135 135 PRO G   49  SER G   61  1                                  13
HELIX  136 136 VAL G   69  THR G   75  5                                   7
HELIX  137 137 SER G   76  LYS G   81  1                                   6
HELIX  138 138 HYP G  104  PHE G  108  5                                   5
HELIX  139 139 SER G  112  GLY G  122  1                                  11
HELIX  140 140 ASN G  123  GLY G  126  5                                   4
HELIX  141 141 PRO G  141  LYS G  146  1                                   6
HELIX  142 142 GLY G  154  ASN G  163  1                                  10
HELIX  143 143 SER G  181  GLY G  195  1                                  15
HELIX  144 144 ARG G  213  GLY G  233  1                                  21
HELIX  145 145 THR G  246  VAL G  255  1                                  10
HELIX  146 146 TYR G  269  GLY G  288  1                                  20
HELIX  147 147 MET G  297  ARG G  303  1                                   7
HELIX  148 148 HIS G  310  GLY G  322  1                                  13
HELIX  149 149 GLU G  338  ASP G  351  1                                  14
HELIX  150 150 ARG G  358  GLY G  361  5                                   4
HELIX  151 151 HIS G  383  TRP G  385  5                                   3
HELIX  152 152 HIS G  386  GLY G  395  1                                  10
HELIX  153 153 GLY G  403  GLY G  408  1                                   6
HELIX  154 154 GLY G  412  GLU G  433  1                                  22
HELIX  155 155 ASP G  436  LYS G  463  1                                  28
HELIX  156 156 TYR H   20  TYR H   25  1                                   6
HELIX  157 157 PRO H   49  SER H   61  1                                  13
HELIX  158 158 VAL H   69  THR H   75  5                                   7
HELIX  159 159 SER H   76  LYS H   81  1                                   6
HELIX  160 160 HYP H  104  PHE H  108  5                                   5
HELIX  161 161 SER H  112  GLY H  122  1                                  11
HELIX  162 162 ASN H  123  GLY H  126  5                                   4
HELIX  163 163 PRO H  141  LYS H  146  1                                   6
HELIX  164 164 GLY H  154  ASN H  163  1                                  10
HELIX  165 165 SER H  181  GLY H  195  1                                  15
HELIX  166 166 ARG H  213  GLY H  233  1                                  21
HELIX  167 167 THR H  246  VAL H  255  1                                  10
HELIX  168 168 TYR H  269  GLY H  288  1                                  20
HELIX  169 169 MET H  297  ARG H  303  1                                   7
HELIX  170 170 HIS H  310  GLY H  322  1                                  13
HELIX  171 171 GLU H  338  ASP H  351  1                                  14
HELIX  172 172 ARG H  358  GLY H  361  5                                   4
HELIX  173 173 HIS H  383  TRP H  385  5                                   3
HELIX  174 174 HIS H  386  GLY H  395  1                                  10
HELIX  175 175 GLY H  403  GLY H  408  1                                   6
HELIX  176 176 GLY H  412  GLU H  433  1                                  22
HELIX  177 177 ASP H  436  LYS H  463  1                                  28
HELIX  178 178 THR I   22  GLY I   37  1                                  16
HELIX  179 179 GLU I   46  ALA I   50  5                                   5
HELIX  180 180 ASN I   54  PHE I   60  5                                   7
HELIX  181 181 ASP I   85  PHE I  100  1                                  16
HELIX  182 182 PRO I  134  ARG I  138  5                                   5
HELIX  183 183 THR J   22  GLY J   37  1                                  16
HELIX  184 184 GLU J   46  ALA J   50  5                                   5
HELIX  185 185 ASN J   54  PHE J   60  5                                   7
HELIX  186 186 ASP J   85  PHE J  100  1                                  16
HELIX  187 187 PRO J  134  ARG J  138  5                                   5
HELIX  188 188 THR K   22  GLY K   37  1                                  16
HELIX  189 189 GLU K   46  ALA K   50  5                                   5
HELIX  190 190 ASN K   54  PHE K   60  5                                   7
HELIX  191 191 ASP K   85  PHE K  100  1                                  16
HELIX  192 192 PRO K  134  ARG K  138  5                                   5
HELIX  193 193 THR L   22  ASN L   36  1                                  15
HELIX  194 194 GLU L   46  ALA L   50  5                                   5
HELIX  195 195 ASN L   54  PHE L   60  5                                   7
HELIX  196 196 ASP L   85  PHE L  100  1                                  16
HELIX  197 197 PRO L  134  ARG L  138  5                                   5
HELIX  198 198 THR M   22  GLY M   37  1                                  16
HELIX  199 199 GLU M   46  ALA M   50  5                                   5
HELIX  200 200 ASN M   54  PHE M   60  5                                   7
HELIX  201 201 ASP M   85  PHE M  100  1                                  16
HELIX  202 202 PRO M  134  ARG M  138  5                                   5
HELIX  203 203 THR N   22  GLY N   37  1                                  16
HELIX  204 204 GLU N   46  ALA N   50  5                                   5
HELIX  205 205 ASN N   54  PHE N   60  5                                   7
HELIX  206 206 ASP N   85  PHE N  100  1                                  16
HELIX  207 207 PRO N  134  ARG N  138  5                                   5
HELIX  208 208 THR O   22  GLY O   37  1                                  16
HELIX  209 209 GLU O   46  ALA O   50  5                                   5
HELIX  210 210 ASN O   54  PHE O   60  5                                   7
HELIX  211 211 ASP O   85  PHE O  100  1                                  16
HELIX  212 212 PRO O  134  ARG O  138  5                                   5
HELIX  213 213 THR P   22  ASN P   36  1                                  15
HELIX  214 214 GLU P   46  ALA P   50  5                                   5
HELIX  215 215 ASN P   54  PHE P   60  5                                   7
HELIX  216 216 ASP P   85  PHE P  100  1                                  16
HELIX  217 217 PRO P  134  ARG P  138  5                                   5
SHEET    1  AA 5 ARG A  83  PRO A  89  0
SHEET    2  AA 5 TYR A  97  TYR A 103 -1  O  ILE A  98   N  GLU A  88
SHEET    3  AA 5 ILE A  36  PRO A  44 -1  O  ILE A  36   N  TYR A 103
SHEET    4  AA 5 LEU A 130  ARG A 139 -1  N  ARG A 131   O  THR A  43
SHEET    5  AA 5 GLY A 308  ILE A 309  1  O  GLY A 308   N  LEU A 135
SHEET    1  AB 8 LEU A 169  GLY A 171  0
SHEET    2  AB 8 CYS A 399  GLN A 401  1  O  LEU A 400   N  GLY A 171
SHEET    3  AB 8 MET A 375  SER A 379  1  O  PRO A 376   N  CYS A 399
SHEET    4  AB 8 HIS A 325  HIS A 327  1  O  LEU A 326   N  VAL A 377
SHEET    5  AB 8 LEU A 290  HIS A 294  1  O  ILE A 293   N  HIS A 327
SHEET    6  AB 8 ILE A 264  ASP A 268  1  O  ILE A 265   N  HIS A 292
SHEET    7  AB 8 GLY A 237  ASN A 241  1  O  LEU A 240   N  MET A 266
SHEET    8  AB 8 PHE A 199  KCX A 201  1  O  THR A 200   N  TYR A 239
SHEET    1  AC 2 TYR A 353  VAL A 354  0
SHEET    2  AC 2 GLN A 366  ASP A 367 -1  O  GLN A 366   N  VAL A 354
SHEET    1  BA 5 ARG B  83  PRO B  89  0
SHEET    2  BA 5 TYR B  97  TYR B 103 -1  O  ILE B  98   N  GLU B  88
SHEET    3  BA 5 ILE B  36  PRO B  44 -1  O  ILE B  36   N  TYR B 103
SHEET    4  BA 5 LEU B 130  ARG B 139 -1  N  ARG B 131   O  THR B  43
SHEET    5  BA 5 GLY B 308  ILE B 309  1  O  GLY B 308   N  LEU B 135
SHEET    1  BB 8 LEU B 169  GLY B 171  0
SHEET    2  BB 8 CYS B 399  GLN B 401  1  O  LEU B 400   N  GLY B 171
SHEET    3  BB 8 MET B 375  SER B 379  1  O  PRO B 376   N  CYS B 399
SHEET    4  BB 8 HIS B 325  HIS B 327  1  O  LEU B 326   N  VAL B 377
SHEET    5  BB 8 LEU B 290  HIS B 294  1  O  ILE B 293   N  HIS B 327
SHEET    6  BB 8 ILE B 264  ASP B 268  1  O  ILE B 265   N  HIS B 292
SHEET    7  BB 8 GLY B 237  ASN B 241  1  O  LEU B 240   N  MET B 266
SHEET    8  BB 8 PHE B 199  KCX B 201  1  O  THR B 200   N  TYR B 239
SHEET    1  BC 2 TYR B 353  VAL B 354  0
SHEET    2  BC 2 GLN B 366  ASP B 367 -1  O  GLN B 366   N  VAL B 354
SHEET    1  CA 5 ARG C  83  PRO C  89  0
SHEET    2  CA 5 TYR C  97  TYR C 103 -1  O  ILE C  98   N  GLU C  88
SHEET    3  CA 5 ILE C  36  PRO C  44 -1  O  ILE C  36   N  TYR C 103
SHEET    4  CA 5 LEU C 130  ARG C 139 -1  N  ARG C 131   O  THR C  43
SHEET    5  CA 5 GLY C 308  ILE C 309  1  O  GLY C 308   N  LEU C 135
SHEET    1  CB 8 LEU C 169  GLY C 171  0
SHEET    2  CB 8 CYS C 399  GLN C 401  1  O  LEU C 400   N  GLY C 171
SHEET    3  CB 8 MET C 375  SER C 379  1  O  PRO C 376   N  CYS C 399
SHEET    4  CB 8 HIS C 325  HIS C 327  1  O  LEU C 326   N  VAL C 377
SHEET    5  CB 8 LEU C 290  HIS C 294  1  O  ILE C 293   N  HIS C 327
SHEET    6  CB 8 ILE C 264  ASP C 268  1  O  ILE C 265   N  HIS C 292
SHEET    7  CB 8 GLY C 237  ASN C 241  1  O  LEU C 240   N  MET C 266
SHEET    8  CB 8 PHE C 199  KCX C 201  1  O  THR C 200   N  TYR C 239
SHEET    1  CC 2 TYR C 353  VAL C 354  0
SHEET    2  CC 2 GLN C 366  ASP C 367 -1  O  GLN C 366   N  VAL C 354
SHEET    1  DA 5 ARG D  83  PRO D  89  0
SHEET    2  DA 5 TYR D  97  TYR D 103 -1  O  ILE D  98   N  GLU D  88
SHEET    3  DA 5 ILE D  36  PRO D  44 -1  O  ILE D  36   N  TYR D 103
SHEET    4  DA 5 LEU D 130  ARG D 139 -1  N  ARG D 131   O  THR D  43
SHEET    5  DA 5 GLY D 308  ILE D 309  1  O  GLY D 308   N  LEU D 135
SHEET    1  DB 8 LEU D 169  GLY D 171  0
SHEET    2  DB 8 CYS D 399  GLN D 401  1  O  LEU D 400   N  GLY D 171
SHEET    3  DB 8 MET D 375  SER D 379  1  O  PRO D 376   N  CYS D 399
SHEET    4  DB 8 HIS D 325  HIS D 327  1  O  LEU D 326   N  VAL D 377
SHEET    5  DB 8 LEU D 290  HIS D 294  1  O  ILE D 293   N  HIS D 327
SHEET    6  DB 8 ILE D 264  ASP D 268  1  O  ILE D 265   N  HIS D 292
SHEET    7  DB 8 GLY D 237  ASN D 241  1  O  LEU D 240   N  MET D 266
SHEET    8  DB 8 PHE D 199  KCX D 201  1  O  THR D 200   N  TYR D 239
SHEET    1  DC 2 TYR D 353  VAL D 354  0
SHEET    2  DC 2 GLN D 366  ASP D 367 -1  O  GLN D 366   N  VAL D 354
SHEET    1  EA 5 ARG E  83  PRO E  89  0
SHEET    2  EA 5 TYR E  97  TYR E 103 -1  O  ILE E  98   N  GLU E  88
SHEET    3  EA 5 ILE E  36  PRO E  44 -1  O  ILE E  36   N  TYR E 103
SHEET    4  EA 5 LEU E 130  ARG E 139 -1  N  ARG E 131   O  THR E  43
SHEET    5  EA 5 GLY E 308  ILE E 309  1  O  GLY E 308   N  LEU E 135
SHEET    1  EB 8 LEU E 169  GLY E 171  0
SHEET    2  EB 8 CYS E 399  GLN E 401  1  O  LEU E 400   N  GLY E 171
SHEET    3  EB 8 MET E 375  SER E 379  1  O  PRO E 376   N  CYS E 399
SHEET    4  EB 8 HIS E 325  HIS E 327  1  O  LEU E 326   N  VAL E 377
SHEET    5  EB 8 LEU E 290  HIS E 294  1  O  ILE E 293   N  HIS E 327
SHEET    6  EB 8 ILE E 264  ASP E 268  1  O  ILE E 265   N  HIS E 292
SHEET    7  EB 8 GLY E 237  ASN E 241  1  O  LEU E 240   N  MET E 266
SHEET    8  EB 8 PHE E 199  KCX E 201  1  O  THR E 200   N  TYR E 239
SHEET    1  EC 2 TYR E 353  VAL E 354  0
SHEET    2  EC 2 GLN E 366  ASP E 367 -1  O  GLN E 366   N  VAL E 354
SHEET    1  FA 5 ARG F  83  PRO F  89  0
SHEET    2  FA 5 TYR F  97  TYR F 103 -1  O  ILE F  98   N  GLU F  88
SHEET    3  FA 5 ILE F  36  PRO F  44 -1  O  ILE F  36   N  TYR F 103
SHEET    4  FA 5 LEU F 130  ARG F 139 -1  N  ARG F 131   O  THR F  43
SHEET    5  FA 5 GLY F 308  ILE F 309  1  O  GLY F 308   N  LEU F 135
SHEET    1  FB 8 LEU F 169  GLY F 171  0
SHEET    2  FB 8 CYS F 399  GLN F 401  1  O  LEU F 400   N  GLY F 171
SHEET    3  FB 8 MET F 375  SER F 379  1  O  PRO F 376   N  CYS F 399
SHEET    4  FB 8 HIS F 325  HIS F 327  1  O  LEU F 326   N  VAL F 377
SHEET    5  FB 8 LEU F 290  HIS F 294  1  O  ILE F 293   N  HIS F 327
SHEET    6  FB 8 ILE F 264  ASP F 268  1  O  ILE F 265   N  HIS F 292
SHEET    7  FB 8 GLY F 237  ASN F 241  1  O  LEU F 240   N  MET F 266
SHEET    8  FB 8 PHE F 199  KCX F 201  1  O  THR F 200   N  TYR F 239
SHEET    1  FC 2 TYR F 353  VAL F 354  0
SHEET    2  FC 2 GLN F 366  ASP F 367 -1  O  GLN F 366   N  VAL F 354
SHEET    1  GA 5 ARG G  83  PRO G  89  0
SHEET    2  GA 5 TYR G  97  TYR G 103 -1  O  ILE G  98   N  GLU G  88
SHEET    3  GA 5 ILE G  36  PRO G  44 -1  O  ILE G  36   N  TYR G 103
SHEET    4  GA 5 LEU G 130  ARG G 139 -1  N  ARG G 131   O  THR G  43
SHEET    5  GA 5 GLY G 308  ILE G 309  1  O  GLY G 308   N  LEU G 135
SHEET    1  GB 8 LEU G 169  GLY G 171  0
SHEET    2  GB 8 CYS G 399  GLN G 401  1  O  LEU G 400   N  GLY G 171
SHEET    3  GB 8 MET G 375  SER G 379  1  O  PRO G 376   N  CYS G 399
SHEET    4  GB 8 HIS G 325  HIS G 327  1  O  LEU G 326   N  VAL G 377
SHEET    5  GB 8 LEU G 290  HIS G 294  1  O  ILE G 293   N  HIS G 327
SHEET    6  GB 8 ILE G 264  ASP G 268  1  O  ILE G 265   N  HIS G 292
SHEET    7  GB 8 GLY G 237  ASN G 241  1  O  LEU G 240   N  MET G 266
SHEET    8  GB 8 PHE G 199  KCX G 201  1  O  THR G 200   N  TYR G 239
SHEET    1  GC 2 TYR G 353  VAL G 354  0
SHEET    2  GC 2 GLN G 366  ASP G 367 -1  O  GLN G 366   N  VAL G 354
SHEET    1  HA 5 ARG H  83  PRO H  89  0
SHEET    2  HA 5 TYR H  97  TYR H 103 -1  O  ILE H  98   N  GLU H  88
SHEET    3  HA 5 ILE H  36  PRO H  44 -1  O  ILE H  36   N  TYR H 103
SHEET    4  HA 5 LEU H 130  ARG H 139 -1  N  ARG H 131   O  THR H  43
SHEET    5  HA 5 GLY H 308  ILE H 309  1  O  GLY H 308   N  LEU H 135
SHEET    1  HB 8 LEU H 169  GLY H 171  0
SHEET    2  HB 8 CYS H 399  GLN H 401  1  O  LEU H 400   N  GLY H 171
SHEET    3  HB 8 MET H 375  SER H 379  1  O  PRO H 376   N  CYS H 399
SHEET    4  HB 8 HIS H 325  HIS H 327  1  O  LEU H 326   N  VAL H 377
SHEET    5  HB 8 LEU H 290  HIS H 294  1  O  ILE H 293   N  HIS H 327
SHEET    6  HB 8 ILE H 264  ASP H 268  1  O  ILE H 265   N  HIS H 292
SHEET    7  HB 8 GLY H 237  ASN H 241  1  O  LEU H 240   N  MET H 266
SHEET    8  HB 8 PHE H 199  KCX H 201  1  O  THR H 200   N  TYR H 239
SHEET    1  HC 2 TYR H 353  VAL H 354  0
SHEET    2  HC 2 GLN H 366  ASP H 367 -1  O  GLN H 366   N  VAL H 354
SHEET    1  IA 4 THR I  74  TRP I  76  0
SHEET    2  IA 4 ILE I  39  ALA I  45 -1  O  LEU I  42   N  TRP I  76
SHEET    3  IA 4 TYR I 104  ASP I 111 -1  O  TYR I 104   N  ALA I  45
SHEET    4  IA 4 VAL I 116  GLN I 124 -1  O  VAL I 116   N  ASP I 111
SHEET    1  JA 4 THR J  74  TRP J  76  0
SHEET    2  JA 4 ILE J  39  ALA J  45 -1  O  LEU J  42   N  TRP J  76
SHEET    3  JA 4 TYR J 104  ASP J 111 -1  O  TYR J 104   N  ALA J  45
SHEET    4  JA 4 VAL J 116  GLN J 124 -1  O  VAL J 116   N  ASP J 111
SHEET    1  KA 4 THR K  74  TRP K  76  0
SHEET    2  KA 4 ILE K  39  ALA K  45 -1  O  LEU K  42   N  TRP K  76
SHEET    3  KA 4 TYR K 104  ASP K 111 -1  O  TYR K 104   N  ALA K  45
SHEET    4  KA 4 VAL K 116  GLN K 124 -1  O  VAL K 116   N  ASP K 111
SHEET    1  LA 4 THR L  74  TRP L  76  0
SHEET    2  LA 4 ILE L  39  ALA L  45 -1  O  LEU L  42   N  TRP L  76
SHEET    3  LA 4 TYR L 104  ASP L 111 -1  O  TYR L 104   N  ALA L  45
SHEET    4  LA 4 VAL L 116  GLN L 124 -1  O  VAL L 116   N  ASP L 111
SHEET    1  MA 4 THR M  74  TRP M  76  0
SHEET    2  MA 4 ILE M  39  ALA M  45 -1  O  LEU M  42   N  TRP M  76
SHEET    3  MA 4 TYR M 104  ASP M 111 -1  O  TYR M 104   N  ALA M  45
SHEET    4  MA 4 VAL M 116  GLN M 124 -1  O  VAL M 116   N  ASP M 111
SHEET    1  NA 4 THR N  74  TRP N  76  0
SHEET    2  NA 4 ILE N  39  ALA N  45 -1  O  LEU N  42   N  TRP N  76
SHEET    3  NA 4 TYR N 104  ASP N 111 -1  O  TYR N 104   N  ALA N  45
SHEET    4  NA 4 VAL N 116  GLN N 124 -1  O  VAL N 116   N  ASP N 111
SHEET    1  OA 4 THR O  74  TRP O  76  0
SHEET    2  OA 4 ILE O  39  ALA O  45 -1  O  LEU O  42   N  TRP O  76
SHEET    3  OA 4 TYR O 104  ASP O 111 -1  O  TYR O 104   N  ALA O  45
SHEET    4  OA 4 VAL O 116  GLN O 124 -1  O  VAL O 116   N  ASP O 111
SHEET    1  PA 4 THR P  74  TRP P  76  0
SHEET    2  PA 4 ILE P  39  ALA P  45 -1  O  LEU P  42   N  TRP P  76
SHEET    3  PA 4 TYR P 104  ASP P 111 -1  O  TYR P 104   N  ALA P  45
SHEET    4  PA 4 VAL P 116  GLN P 124 -1  O  VAL P 116   N  ASP P 111
SSBOND   1 CYS A  247    CYS B  247                          1555   1555  2.08
SSBOND   2 CYS C  247    CYS D  247                          1555   1555  2.08
SSBOND   3 CYS E  247    CYS F  247                          1555   1555  2.07
SSBOND   4 CYS G  247    CYS H  247                          1555   1555  2.09
LINK         C   TYR A 103                 N   HYP A 104     1555   1555  1.35
LINK         C   HYP A 104                 N   ILE A 105     1555   1555  1.33
LINK         C   GLY A 150                 N   HYP A 151     1555   1555  1.34
LINK         C   HYP A 151                 N   PRO A 152     1555   1555  1.35
LINK         C   THR A 200                 N   KCX A 201     1555   1555  1.33
LINK         C   KCX A 201                 N   ASP A 202     1555   1555  1.33
LINK         C   VAL A 255                 N   SMC A 256     1555   1555  1.33
LINK         C   SMC A 256                 N   ALA A 257     1555   1555  1.33
LINK         C   TRP A 368                 N   SMC A 369     1555   1555  1.33
LINK         C   SMC A 369                 N   SER A 370     1555   1555  1.33
LINK        MG    MG A 477                 OQ1 KCX A 201     1555   1555  2.02
LINK        MG    MG A 477                 OD1 ASP A 203     1555   1555  1.98
LINK        MG    MG A 477                 O2  CAP A 476     1555   1555  2.25
LINK        MG    MG A 477                 OE1 GLU A 204     1555   1555  2.03
LINK        MG    MG A 477                 O3  CAP A 476     1555   1555  2.14
LINK        MG    MG A 477                 O7  CAP A 476     1555   1555  2.11
LINK         C   TYR B 103                 N   HYP B 104     1555   1555  1.35
LINK         C   HYP B 104                 N   ILE B 105     1555   1555  1.33
LINK         C   GLY B 150                 N   HYP B 151     1555   1555  1.34
LINK         C   HYP B 151                 N   PRO B 152     1555   1555  1.34
LINK         C   THR B 200                 N   KCX B 201     1555   1555  1.33
LINK         C   KCX B 201                 N   ASP B 202     1555   1555  1.34
LINK         C   VAL B 255                 N   SMC B 256     1555   1555  1.34
LINK         C   SMC B 256                 N   ALA B 257     1555   1555  1.33
LINK         C   TRP B 368                 N   SMC B 369     1555   1555  1.33
LINK         C   SMC B 369                 N   SER B 370     1555   1555  1.34
LINK        MG    MG B 476                 OQ1 KCX B 201     1555   1555  1.99
LINK        MG    MG B 476                 O2  CAP B 477     1555   1555  2.27
LINK        MG    MG B 476                 O3  CAP B 477     1555   1555  2.07
LINK        MG    MG B 476                 OD1 ASP B 203     1555   1555  2.03
LINK        MG    MG B 476                 OE1 GLU B 204     1555   1555  2.01
LINK        MG    MG B 476                 O7  CAP B 477     1555   1555  2.24
LINK         C   TYR C 103                 N   HYP C 104     1555   1555  1.34
LINK         C   HYP C 104                 N   ILE C 105     1555   1555  1.33
LINK         C   GLY C 150                 N   HYP C 151     1555   1555  1.34
LINK         C   HYP C 151                 N   PRO C 152     1555   1555  1.34
LINK         C   THR C 200                 N   KCX C 201     1555   1555  1.33
LINK         C   KCX C 201                 N   ASP C 202     1555   1555  1.34
LINK         C   VAL C 255                 N   SMC C 256     1555   1555  1.33
LINK         C   SMC C 256                 N   ALA C 257     1555   1555  1.33
LINK         C   TRP C 368                 N   SMC C 369     1555   1555  1.33
LINK         C   SMC C 369                 N   SER C 370     1555   1555  1.33
LINK        MG    MG C 476                 O3  CAP C 477     1555   1555  2.11
LINK        MG    MG C 476                 OQ1 KCX C 201     1555   1555  1.95
LINK        MG    MG C 476                 OD1 ASP C 203     1555   1555  1.97
LINK        MG    MG C 476                 O2  CAP C 477     1555   1555  2.33
LINK        MG    MG C 476                 OE1 GLU C 204     1555   1555  1.98
LINK        MG    MG C 476                 O7  CAP C 477     1555   1555  2.17
LINK         C   TYR D 103                 N   HYP D 104     1555   1555  1.34
LINK         C   HYP D 104                 N   ILE D 105     1555   1555  1.33
LINK         C   GLY D 150                 N   HYP D 151     1555   1555  1.35
LINK         C   HYP D 151                 N   PRO D 152     1555   1555  1.34
LINK         C   THR D 200                 N   KCX D 201     1555   1555  1.32
LINK         C   KCX D 201                 N   ASP D 202     1555   1555  1.33
LINK         C   VAL D 255                 N   SMC D 256     1555   1555  1.33
LINK         C   SMC D 256                 N   ALA D 257     1555   1555  1.33
LINK         C   TRP D 368                 N   SMC D 369     1555   1555  1.33
LINK         C   SMC D 369                 N   SER D 370     1555   1555  1.33
LINK        MG    MG D 476                 O7  CAP D 477     1555   1555  2.14
LINK        MG    MG D 476                 O2  CAP D 477     1555   1555  2.24
LINK        MG    MG D 476                 O3  CAP D 477     1555   1555  2.13
LINK        MG    MG D 476                 OQ1 KCX D 201     1555   1555  1.97
LINK        MG    MG D 476                 OE1 GLU D 204     1555   1555  2.08
LINK        MG    MG D 476                 OD1 ASP D 203     1555   1555  1.96
LINK         C   TYR E 103                 N   HYP E 104     1555   1555  1.35
LINK         C   HYP E 104                 N   ILE E 105     1555   1555  1.33
LINK         C   GLY E 150                 N   HYP E 151     1555   1555  1.35
LINK         C   HYP E 151                 N   PRO E 152     1555   1555  1.34
LINK         C   THR E 200                 N   KCX E 201     1555   1555  1.33
LINK         C   KCX E 201                 N   ASP E 202     1555   1555  1.33
LINK         C   VAL E 255                 N   SMC E 256     1555   1555  1.33
LINK         C   SMC E 256                 N   ALA E 257     1555   1555  1.33
LINK         C   TRP E 368                 N   SMC E 369     1555   1555  1.33
LINK         C   SMC E 369                 N   SER E 370     1555   1555  1.33
LINK        MG    MG E 476                 OQ1 KCX E 201     1555   1555  1.99
LINK        MG    MG E 476                 OD1 ASP E 203     1555   1555  1.97
LINK        MG    MG E 476                 O7  CAP E 477     1555   1555  2.14
LINK        MG    MG E 476                 OE1 GLU E 204     1555   1555  2.05
LINK        MG    MG E 476                 O3  CAP E 477     1555   1555  2.13
LINK        MG    MG E 476                 O2  CAP E 477     1555   1555  2.24
LINK         C   TYR F 103                 N   HYP F 104     1555   1555  1.35
LINK         C   HYP F 104                 N   ILE F 105     1555   1555  1.33
LINK         C   GLY F 150                 N   HYP F 151     1555   1555  1.34
LINK         C   HYP F 151                 N   PRO F 152     1555   1555  1.35
LINK         C   THR F 200                 N   KCX F 201     1555   1555  1.32
LINK         C   KCX F 201                 N   ASP F 202     1555   1555  1.33
LINK         C   VAL F 255                 N   SMC F 256     1555   1555  1.34
LINK         C   SMC F 256                 N   ALA F 257     1555   1555  1.33
LINK         C   TRP F 368                 N   SMC F 369     1555   1555  1.33
LINK         C   SMC F 369                 N   SER F 370     1555   1555  1.34
LINK        MG    MG F 476                 OE1 GLU F 204     1555   1555  2.01
LINK        MG    MG F 476                 O3  CAP F 477     1555   1555  2.16
LINK        MG    MG F 476                 OQ1 KCX F 201     1555   1555  1.98
LINK        MG    MG F 476                 O7  CAP F 477     1555   1555  2.13
LINK        MG    MG F 476                 O2  CAP F 477     1555   1555  2.28
LINK        MG    MG F 476                 OD1 ASP F 203     1555   1555  1.96
LINK         C   TYR G 103                 N   HYP G 104     1555   1555  1.35
LINK         C   HYP G 104                 N   ILE G 105     1555   1555  1.33
LINK         C   GLY G 150                 N   HYP G 151     1555   1555  1.34
LINK         C   HYP G 151                 N   PRO G 152     1555   1555  1.34
LINK         C   THR G 200                 N   KCX G 201     1555   1555  1.33
LINK         C   KCX G 201                 N   ASP G 202     1555   1555  1.33
LINK         C   VAL G 255                 N   SMC G 256     1555   1555  1.33
LINK         C   SMC G 256                 N   ALA G 257     1555   1555  1.33
LINK         C   TRP G 368                 N   SMC G 369     1555   1555  1.33
LINK         C   SMC G 369                 N   SER G 370     1555   1555  1.33
LINK        MG    MG G 476                 OD1 ASP G 203     1555   1555  1.95
LINK        MG    MG G 476                 O2  CAP G 477     1555   1555  2.25
LINK        MG    MG G 476                 O7  CAP G 477     1555   1555  2.21
LINK        MG    MG G 476                 OQ1 KCX G 201     1555   1555  1.96
LINK        MG    MG G 476                 O3  CAP G 477     1555   1555  2.15
LINK        MG    MG G 476                 OE1 GLU G 204     1555   1555  1.96
LINK         C   TYR H 103                 N   HYP H 104     1555   1555  1.35
LINK         C   HYP H 104                 N   ILE H 105     1555   1555  1.33
LINK         C   GLY H 150                 N   HYP H 151     1555   1555  1.34
LINK         C   HYP H 151                 N   PRO H 152     1555   1555  1.35
LINK         C   THR H 200                 N   KCX H 201     1555   1555  1.33
LINK         C   KCX H 201                 N   ASP H 202     1555   1555  1.33
LINK         C   VAL H 255                 N   SMC H 256     1555   1555  1.33
LINK         C   SMC H 256                 N   ALA H 257     1555   1555  1.33
LINK         C   TRP H 368                 N   SMC H 369     1555   1555  1.33
LINK         C   SMC H 369                 N   SER H 370     1555   1555  1.33
LINK        MG    MG H 476                 OE1 GLU H 204     1555   1555  2.03
LINK        MG    MG H 476                 OD1 ASP H 203     1555   1555  2.02
LINK        MG    MG H 476                 O7  CAP H 477     1555   1555  2.13
LINK        MG    MG H 476                 O2  CAP H 477     1555   1555  2.28
LINK        MG    MG H 476                 OQ1 KCX H 201     1555   1555  1.97
LINK        MG    MG H 476                 O3  CAP H 477     1555   1555  2.17
LINK         C   MME I   1                 N   MET I   2     1555   1555  1.33
LINK         C   MME J   1                 N   MET J   2     1555   1555  1.33
LINK         C   MME K   1                 N   MET K   2     1555   1555  1.33
LINK         C   MME L   1                 N   MET L   2     1555   1555  1.33
LINK         C   MME M   1                 N   MET M   2     1555   1555  1.33
LINK         C   MME N   1                 N   MET N   2     1555   1555  1.33
LINK         C   MME O   1                 N   MET O   2     1555   1555  1.33
LINK         C   MME P   1                 N   MET P   2     1555   1555  1.33
CISPEP   1 LYS A  175    PRO A  176          0        -0.81
CISPEP   2 LYS B  175    PRO B  176          0         0.38
CISPEP   3 LYS C  175    PRO C  176          0        -1.96
CISPEP   4 LYS D  175    PRO D  176          0        -0.56
CISPEP   5 LYS E  175    PRO E  176          0        -1.12
CISPEP   6 LYS F  175    PRO F  176          0        -3.57
CISPEP   7 LYS G  175    PRO G  176          0        -0.77
CISPEP   8 LYS H  175    PRO H  176          0        -1.19
SITE     1 AC1 28 THR A 173  LYS A 175  LYS A 177  KCX A 201
SITE     2 AC1 28 ASP A 203  GLU A 204  HIS A 294  ARG A 295
SITE     3 AC1 28 HIS A 327  LYS A 334  LEU A 335  SER A 379
SITE     4 AC1 28 GLY A 380  GLY A 381  GLY A 403  GLY A 404
SITE     5 AC1 28  MG A 477  HOH A2125  HOH A2244  HOH A2289
SITE     6 AC1 28 HOH A2290  HOH A2291  HOH A2292  GLU B  60
SITE     7 AC1 28 THR B  65  TRP B  66  ASN B 123  HOH B2034
SITE     1 AC2  5 LYS A 177  KCX A 201  ASP A 203  GLU A 204
SITE     2 AC2  5 CAP A 476
SITE     1 AC3  4 KCX B 201  ASP B 203  GLU B 204  CAP B 477
SITE     1 AC4 30 GLU A  60  THR A  65  TRP A  66  ASN A 123
SITE     2 AC4 30 HOH A2091  HOH A2092  THR B 173  LYS B 175
SITE     3 AC4 30 LYS B 177  KCX B 201  ASP B 203  GLU B 204
SITE     4 AC4 30 HIS B 294  ARG B 295  HIS B 327  LYS B 334
SITE     5 AC4 30 LEU B 335  SER B 379  GLY B 380  GLY B 381
SITE     6 AC4 30 GLY B 403  GLY B 404   MG B 476  HOH B2115
SITE     7 AC4 30 HOH B2116  HOH B2233  HOH B2279  HOH B2280
SITE     8 AC4 30 HOH B2281  HOH B2282
SITE     1 AC5  4 KCX C 201  ASP C 203  GLU C 204  CAP C 477
SITE     1 AC6 30 THR C 173  LYS C 175  LYS C 177  KCX C 201
SITE     2 AC6 30 ASP C 203  GLU C 204  HIS C 294  ARG C 295
SITE     3 AC6 30 HIS C 327  LYS C 334  LEU C 335  SER C 379
SITE     4 AC6 30 GLY C 380  GLY C 381  GLY C 403  GLY C 404
SITE     5 AC6 30  MG C 476  HOH C2120  HOH C2121  HOH C2226
SITE     6 AC6 30 HOH C2239  HOH C2273  HOH C2274  HOH C2275
SITE     7 AC6 30 GLU D  60  THR D  65  TRP D  66  ASN D 123
SITE     8 AC6 30 HOH D2034  HOH D2085
SITE     1 AC7  5 LYS D 177  KCX D 201  ASP D 203  GLU D 204
SITE     2 AC7  5 CAP D 477
SITE     1 AC8 30 GLU C  60  THR C  65  TRP C  66  ASN C 123
SITE     2 AC8 30 HOH C2038  HOH C2088  THR D 173  LYS D 175
SITE     3 AC8 30 LYS D 177  KCX D 201  ASP D 203  GLU D 204
SITE     4 AC8 30 HIS D 294  ARG D 295  HIS D 327  LYS D 334
SITE     5 AC8 30 LEU D 335  SER D 379  GLY D 380  GLY D 381
SITE     6 AC8 30 GLY D 403  GLY D 404   MG D 476  HOH D2119
SITE     7 AC8 30 HOH D2120  HOH D2256  HOH D2257  HOH D2258
SITE     8 AC8 30 HOH D2259  HOH D2260
SITE     1 AC9  5 LYS E 177  KCX E 201  ASP E 203  GLU E 204
SITE     2 AC9  5 CAP E 477
SITE     1 BC1 28 THR E 173  LYS E 175  LYS E 177  KCX E 201
SITE     2 BC1 28 ASP E 203  GLU E 204  HIS E 294  ARG E 295
SITE     3 BC1 28 HIS E 327  LYS E 334  LEU E 335  SER E 379
SITE     4 BC1 28 GLY E 380  GLY E 381  GLY E 403  GLY E 404
SITE     5 BC1 28  MG E 476  HOH E2096  HOH E2205  HOH E2220
SITE     6 BC1 28 HOH E2259  HOH E2260  HOH E2261  GLU F  60
SITE     7 BC1 28 THR F  65  TRP F  66  ASN F 123  HOH F2078
SITE     1 BC2  5 LYS F 177  KCX F 201  ASP F 203  GLU F 204
SITE     2 BC2  5 CAP F 477
SITE     1 BC3 29 GLU E  60  THR E  65  TRP E  66  ASN E 123
SITE     2 BC3 29 HOH E2023  HOH E2061  THR F 173  LYS F 175
SITE     3 BC3 29 LYS F 177  KCX F 201  ASP F 203  GLU F 204
SITE     4 BC3 29 HIS F 294  ARG F 295  HIS F 327  LYS F 334
SITE     5 BC3 29 LEU F 335  SER F 379  GLY F 380  GLY F 381
SITE     6 BC3 29 GLY F 403  GLY F 404   MG F 476  HOH F2245
SITE     7 BC3 29 HOH F2246  HOH F2247  HOH F2248  HOH F2249
SITE     8 BC3 29 HOH F2250
SITE     1 BC4  5 LYS G 177  KCX G 201  ASP G 203  GLU G 204
SITE     2 BC4  5 CAP G 477
SITE     1 BC5 29 THR G 173  LYS G 175  LYS G 177  KCX G 201
SITE     2 BC5 29 ASP G 203  GLU G 204  HIS G 294  ARG G 295
SITE     3 BC5 29 HIS G 327  LYS G 334  LEU G 335  SER G 379
SITE     4 BC5 29 GLY G 380  GLY G 381  GLY G 403  GLY G 404
SITE     5 BC5 29  MG G 476  HOH G2121  HOH G2227  HOH G2279
SITE     6 BC5 29 HOH G2280  HOH G2281  HOH G2282  GLU H  60
SITE     7 BC5 29 THR H  65  TRP H  66  ASN H 123  HOH H2038
SITE     8 BC5 29 HOH H2088
SITE     1 BC6  5 LYS H 177  KCX H 201  ASP H 203  GLU H 204
SITE     2 BC6  5 CAP H 477
SITE     1 BC7 30 GLU G  60  THR G  65  TRP G  66  ASN G 123
SITE     2 BC7 30 HOH G2038  HOH G2082  THR H 173  LYS H 175
SITE     3 BC7 30 LYS H 177  KCX H 201  ASP H 203  GLU H 204
SITE     4 BC7 30 HIS H 294  ARG H 295  HIS H 327  LYS H 334
SITE     5 BC7 30 LEU H 335  SER H 379  GLY H 380  GLY H 381
SITE     6 BC7 30 GLY H 403  GLY H 404   MG H 476  HOH H2119
SITE     7 BC7 30 HOH H2120  HOH H2234  HOH H2245  HOH H2277
SITE     8 BC7 30 HOH H2278  HOH H2279
SITE     1 BC8  8 VAL A  17  LYS A  18  THR A  65  TRP A  66
SITE     2 BC8  8 THR A  67  THR A  68  HOH A2014  HOH A2293
SITE     1 BC9  2 GLU A  52  HOH A2294
SITE     1 CC1  7 ARG A 295  SER A 328  GLY A 329  GLU A 336
SITE     2 CC1  7 PHE A 345  HOH A2193  HOH A2295
SITE     1 CC2  4 LYS H 466  GLU H 468  PHE H 469  HOH H2281
SITE     1 CC3  8 ARG H 295  HIS H 298  ASP H 302  PHE H 311
SITE     2 CC3  8 SER H 328  GLU H 336  PHE H 345  HOH H2199
SITE     1 CC4  4 TYR A 226  LYS O  49  GLU O  55  HOH O2079
SITE     1 CC5  6 GLY O  37  TRP O  38  PHE O  81  GLY O  82
SITE     2 CC5  6 CYS O  83  HOH O2081
SITE     1 CC6  8 VAL C  17  LYS C  18  THR C  65  TRP C  66
SITE     2 CC6  8 THR C  67  THR C  68  HOH C2021  HOH C2040
SITE     1 CC7  5 GLY K  37  TRP K  38  ILE K  39  GLY K  82
SITE     2 CC7  5 CYS K  83
SITE     1 CC8  9 TYR B  24  GLY B  64  THR B  68  VAL B  69
SITE     2 CC8  9 ASP B  72  EDO B1476  HOH B2283  HOH B2284
SITE     3 CC8  9 HOH B2285
SITE     1 CC9  9 VAL B  17  LYS B  18  THR B  65  TRP B  66
SITE     2 CC9  9 THR B  67  THR B  68  EDO B1475  HOH B2283
SITE     3 CC9  9 HOH B2286
SITE     1 DC1  3 PHE A 469  HOH A2296  TYR B  20
SITE     1 DC2  5 HOH A2294  LYS B 466  PHE B 467  GLU B 468
SITE     2 DC2  5 PHE B 469
SITE     1 DC3  6 TYR H 226  ALA H 230  LYS J  49  GLU J  55
SITE     2 DC3  6 ASP J  69  HOH J2083
SITE     1 DC4  6 LEU G 270  GLY G 273  PHE G 274  HOH G2287
SITE     2 DC4  6 LEU H 270  THR H 271
SITE     1 DC5  8 LYS D  18  THR D  65  TRP D  66  THR D  67
SITE     2 DC5  8 THR D  68  EDO D1477  HOH D2037  HOH D2261
SITE     1 DC6  5 LYS D 466  PHE D 467  GLU D 468  PHE D 469
SITE     2 DC6  5 HOH D2262
SITE     1 DC7  6 TYR E  24  THR E  68  VAL E  69  ASP E  72
SITE     2 DC7  6 HOH E2026  HOH E2262
SITE     1 DC8  4 LYS E 466  PHE E 467  GLU E 468  PHE E 469
SITE     1 DC9  6 GLY J  37  TRP J  38  PHE J  81  GLY J  82
SITE     2 DC9  6 CYS J  83  HOH J2084
SITE     1 EC1  8 TYR D  24  THR D  68  VAL D  69  ASP D  72
SITE     2 EC1  8 EDO D1475  HOH D2036  HOH D2037  HOH D2045
SITE     1 EC2  5 ARG D 295  PHE D 311  GLY D 329  GLU D 336
SITE     2 EC2  5 HOH D2191
SITE     1 EC3  5 TYR F 226  LYS P  49  GLU P  55  HOH P2045
SITE     2 EC3  5 HOH P2077
SITE     1 EC4  6 TYR D 226  HOH D2146  LYS N  49  GLU N  55
SITE     2 EC4  6 ASP N  69  HOH N2033
SITE     1 EC5  6 GLY N  37  ILE N  39  PHE N  81  GLY N  82
SITE     2 EC5  6 CYS N  83  HOH N2072
SITE     1 EC6  7 TYR B 226  LYS B 227  HOH B2142  LYS L  49
SITE     2 EC6  7 GLU L  55  SER L  56  ASP L  69
SITE     1 EC7  5 GLY A  10  HOH A2051  GLY L  37  ILE L  39
SITE     2 EC7  5 GLY L  82
SITE     1 EC8  4 LYS A 466  GLU A 468  PHE A 469  HOH A2296
SITE     1 EC9  4 TYR C  20  GLU C  52  HOH C2277  HOH C2278
SITE     1 FC1  6 LYS C 466  PHE C 467  GLU C 468  PHE C 469
SITE     2 FC1  6 HOH C2279  HOH C2280
SITE     1 FC2  5 ARG C 295  PHE C 345  ASP C 473  HOH C2281
SITE     2 FC2  5 HOH C2282
SITE     1 FC3  3 TYR G  20  GLU G  52  HOH H2281
SITE     1 FC4  5 TYR C 226  LYS I  49  GLU I  55  HOH I2039
SITE     2 FC4  5 HOH I2075
SITE     1 FC5  5 TYR E 226  HOH E2126  LYS K  49  GLU K  55
SITE     2 FC5  5 HOH K2051
SITE     1 FC6  5 TYR G 226  LYS M  49  GLU M  55  HOH M2056
SITE     2 FC6  5 HOH M2103
SITE     1 FC7  8 GLY H  10  GLY M  37  ILE M  39  PHE M  81
SITE     2 FC7  8 GLY M  82  HOH M2104  HOH M2105  HOH M2106
SITE     1 FC8  4 LEU C 270  HOH C2276  LEU D 270  HOH D2167
SITE     1 FC9  7 LYS H  18  THR H  65  TRP H  66  THR H  67
SITE     2 FC9  7 THR H  68  HOH H2019  HOH H2280
SITE     1 GC1  1 GLU H  52
SITE     1 GC2  9 TYR G  24  GLY G  64  THR G  68  VAL G  69
SITE     2 GC2  9 ASP G  72  EDO G1476  HOH G2283  HOH G2284
SITE     3 GC2  9 HOH G2285
SITE     1 GC3  8 LYS G  18  THR G  65  TRP G  66  THR G  67
SITE     2 GC3  8 THR G  68  EDO G1475  HOH G2013  HOH G2284
SITE     1 GC4  5 LYS G 466  PHE G 467  GLU G 468  PHE G 469
SITE     2 GC4  5 HOH G2286
SITE     1 GC5  3 ARG G 295  PHE G 345  ASP G 473
SITE     1 GC6  7 LYS E  18  THR E  65  TRP E  66  THR E  67
SITE     2 GC6  7 THR E  68  HOH E2006  HOH E2026
SITE     1 GC7  7 LYS F  18  THR F  65  TRP F  66  THR F  67
SITE     2 GC7  7 THR F  68  HOH F2251  HOH F2252
SITE     1 GC8  2 GLU F  52  HOH F2253
CRYST1  121.377  177.446  122.568  90.00 117.65  90.00 P 1 21 1     16
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.008239  0.000000  0.004316        0.00000
SCALE2      0.000000  0.005636  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009211        0.00000
      
PROCHECK
Go to PROCHECK summary
 References